| Autor: |
Haratipour Z; Department of Chemistry and Biochemistry, Old Dominion University, Norfolk, VA, 23529, USA., Aldabagh H; Department of Computer Science, Old Dominion University, Norfolk, VA, 23529, USA., Li Y; Department of Computer Science, Old Dominion University, Norfolk, VA, 23529, USA., Greene LH; Department of Chemistry and Biochemistry, Old Dominion University, Norfolk, VA, 23529, USA. lgreene@odu.edu. |
| Abstrakt: |
Understanding and computationally predicting the protein folding process remains one of the most challenging scientific problems and has uniquely garnered the interdisciplinary efforts of researchers from both the biological, chemical, physical and computational disciplines. Previous studies have demonstrated the importance of long-range interactions in guiding the native structure. However, predicting how the native long-range interaction network forms to generate a specific topology from among all other conformations remains unresolved. The present research study conducts an exploratory study to identify amino acids and long-range interactions that have the potential to play a key role in building and maintaining the protein topology. Towards this end, the application of network science is utilized and developed to analyze the structures of a group of proteins that share a common Greek-key topology but differ in sequence, secondary structure and function. We investigate the idea that the residues with high betweeness centrality score are potentially significant in maintaining the protein network and in governing the Greek-key topology. This hypothesis is tested by two different computational methods: through a fragmentation test and by the analysis of diameter impacts. In summary, we find a subset of selected residues in similar geographical positions in all model proteins, which demonstrates the role of these specific residues and regions in governing the Greek-key topology from a network perspective. |
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